Related Experiment Video
Updated: May 5, 2026

Enrichment of Native and Recombinant Extracellular Vesicles of Mycobacteria
Published on: December 8, 2023
Cloning, expression, purification, crystallization and preliminary X-ray studies of argininosuccinate lyase (Rv1659)
1Molecular Biophysics Unit, Indian Institute of Science, Bangalore 560 012, India.
Abstract:
The last enzyme in the arginine-biosynthesis pathway, argininosuccinate lyase, from Mycobacterium tuberculosis has been cloned, expressed, purified and crystallized, and preliminary X-ray studies have been carried out on the crystals. The His-tagged tetrameric enzyme with a subunit molecular weight of 50.9 kDa crystallized with two tetramers in the asymmetric unit of the orthorhombic unit cell, space group P2(1)2(1)2(1). Molecular-replacement calculations and self-rotation calculations confirmed the space group and the tetrameric nature of the molecule.
More Related Videos
09:29Mycobacterium tuberculosis Extracellular Vesicle Enrichment through Size Exclusion Chromatography
Published on: May 19, 2022
12:23Recombinant Protein Expression, Crystallization, and Biophysical Studies of a Bacillus-conserved Nucleotide Pyrophosphorylase, BcMazG
Published on: May 16, 2017